dbPTM

IKBE_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IKBE_HUMAN
UniProt AC	O00221
Protein Name	NF-kappa-B inhibitor epsilon
Gene Name	NFKBIE
Organism	Homo sapiens (Human).
Sequence Length	500
Subcellular Localization	Cytoplasm.
Protein Description	Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. Inhibits DNA-binding of NF-kappa-B p50-p65 and p50-c-Rel complexes..
Protein Sequence	MNQRRSESRPGNHRLQAYAEPGKGDSGGAGPLSGSARRGRGGGGAIRVRRPCWSGGAGRGGGPAWAVRLPTVTAGWTWPALRTLSSLRAGPSEPHSPGRRPPRAGRPLCQADPQPGKAARRSLEPDPAQTGPRPARAAGMSEARKGPDEAEESQYDSGIESLRSLRSLPESTSAPASGPSDGSPQPCTHPPGPVKEPQEKEDADGERADSTYGSSSLTYTLSLLGGPEAEDPAPRLPLPHVGALSPQQLEALTYISEDGDTLVHLAVIHEAPAVLLCCLALLPQEVLDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLEGRPEPGRGTSHSLDLQLQNWQGLACLHIATLQKNQPLMELLLRNGADIDVQEGTSGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRGLMGISSTLCKAGADSLLRNVEDETPQDLTEESLVLLPFDDLKISGKLLLCTD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
54	Phosphorylation	RVRRPCWSGGAGRGG EEECCCCCCCCCCCC	33.78	-
85	Phosphorylation	WPALRTLSSLRAGPS HHHHHHHHHHCCCCC	27.06	30301811
86	Phosphorylation	PALRTLSSLRAGPSE HHHHHHHHHCCCCCC	25.61	25954137
130	Phosphorylation	LEPDPAQTGPRPARA CCCCHHHCCCCCCHH	51.78	22210691
153	Phosphorylation	GPDEAEESQYDSGIE CCCHHHHHHHHHHHH	26.08	25106551
155	Phosphorylation	DEAEESQYDSGIESL CHHHHHHHHHHHHHH	22.73	28674151
157	Phosphorylation	AEESQYDSGIESLRS HHHHHHHHHHHHHHH	36.41	23401153
161	Phosphorylation	QYDSGIESLRSLRSL HHHHHHHHHHHHHCC	27.45	28450419
164	Phosphorylation	SGIESLRSLRSLPES HHHHHHHHHHCCCCC	33.17	28555341
167	Phosphorylation	ESLRSLRSLPESTSA HHHHHHHCCCCCCCC	54.27	25850435
171	Phosphorylation	SLRSLPESTSAPASG HHHCCCCCCCCCCCC	26.23	25850435
172	Phosphorylation	LRSLPESTSAPASGP HHCCCCCCCCCCCCC	27.52	29978859
173	Phosphorylation	RSLPESTSAPASGPS HCCCCCCCCCCCCCC	41.35	29978859
177	Phosphorylation	ESTSAPASGPSDGSP CCCCCCCCCCCCCCC	50.61	21712546
180	Phosphorylation	SAPASGPSDGSPQPC CCCCCCCCCCCCCCC	59.12	23663014
183	Phosphorylation	ASGPSDGSPQPCTHP CCCCCCCCCCCCCCC	25.92	25159151
188	Phosphorylation	DGSPQPCTHPPGPVK CCCCCCCCCCCCCCC	44.06	23663014
214	Phosphorylation	RADSTYGSSSLTYTL CCCCCCCCCCCEEEE	13.31	27251275
215	Phosphorylation	ADSTYGSSSLTYTLS CCCCCCCCCCEEEEE	25.63	26657352
216	Phosphorylation	DSTYGSSSLTYTLSL CCCCCCCCCEEEEEH	26.82	26657352
218	Phosphorylation	TYGSSSLTYTLSLLG CCCCCCCEEEEEHHC	19.19	27251275
316	Ubiquitination	AVRALVLKGASRALQ HHHHHHHHHHHHHHH	44.97	-
463	Phosphorylation	LCKAGADSLLRNVED HHHHCHHHHHHCCCC	28.86	24719451
494	Acetylation	DDLKISGKLLLCTD- HHCEECCEEEEECC-	29.22	25953088

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:25503564
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IKBE_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
188	Phosphorylation	194 (6)	V ⇒ A	rs2233434	Rheumatoid arthritis	22446963 23028356

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NFKB1_HUMAN	NFKB1	physical	9315679
TF65_HUMAN	RELA	physical	9315679
REL_HUMAN	REL	physical	9315679
NFKB2_HUMAN	NFKB2	physical	9315679
NCOR2_HUMAN	NCOR2	physical	15536134
HDAC4_HUMAN	HDAC4	physical	15536134
HDAC5_HUMAN	HDAC5	physical	15536134
TF65_HUMAN	RELA	physical	21988832
FBW1A_HUMAN	BTRC	physical	10497169

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of IKBE_HUMAN

Related Literatures of Post-Translational Modification